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Related Concept Videos

NMR Spectroscopy: Chemical Shift Overview01:15

NMR Spectroscopy: Chemical Shift Overview

The position of the absorption signal of a sample is reported relative to the position of the signal of tetramethylsilane (TMS), which is added as an internal reference while recording spectra. The difference between the absorption frequencies of the sample and TMS (in Hz) is divided by the spectrometer operating frequency (in MHz) to obtain a dimensionless quantity called the chemical shift. It is reported on the δ (delta) scale and expressed in parts per million.
For instance, the proton...
¹H NMR: Interpreting Distorted and Overlapping Signals01:02

¹H NMR: Interpreting Distorted and Overlapping Signals

Spin systems where the difference in chemical shifts of the coupled nuclei is greater than ten times J are called first-order spin systems. These nuclei are weakly coupled, and their chemical shifts and coupling constant can generally be estimated from the well-separated signals in the spectrum.
As Δν decreases and the signals move closer, the doublets appear increasingly distorted. The intensities of the inner lines increase at the cost of those of the outer lines as the signals are slanted or...
Chemical Shift: Internal References and Solvent Effects01:17

Chemical Shift: Internal References and Solvent Effects

In an NMR sample, precise measurement of the absolute absorption frequencies of nuclei is difficult. A standard internal reference compound is added, and the frequency difference between the reference signal and sample signals is measured.
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
Proton (¹H) NMR: Chemical Shift01:07

Proton (¹H) NMR: Chemical Shift

Organic molecules primarily contain carbon and hydrogen atoms. While all the hydrogen isotopes are NMR-active, protium or hydrogen-1 is the most abundant. It has a significant energy separation between its nuclear spin states due to its large gyromagnetic ratio. As per Boltzmann's distribution, an increase in the energy separation implies a greater excess population of nuclei available for excitation, resulting in a strong NMR absorption signal.
Absorption signals of all the protium nuclei in a...
NMR Spectroscopy Of Amines01:19

NMR Spectroscopy Of Amines

In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is broad and...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Using chemical shifts to determine structural changes in proteins upon complex formation.

Andrea Cavalli1, Rinaldo W Montalvao, Michele Vendruscolo

  • 1Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.

The Journal of Physical Chemistry. B
|June 7, 2011
PubMed
Summary

Determining protein structures with chemical shifts is improving. This study presents a new method to accurately track conformational changes in protein complexes, even with small binding-induced chemical shift changes.

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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Published on: September 17, 2017

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Chemistry

Background:

  • Protein structure determination using chemical shifts is advancing.
  • Limited chemical shift changes upon protein complex formation pose a challenge for structural analysis.
  • Existing methods struggle with small, often ambiguous, chemical shift perturbations.

Purpose of the Study:

  • To develop a reliable method for determining protein complex structures.
  • To accurately identify conformational changes during complex formation using chemical shifts.
  • To overcome the limitations of small chemical shift variations in structural analysis.

Main Methods:

  • Utilizing a novel procedure for analyzing chemical shift data.
  • Applying the method to protein complexes with subtle binding-induced changes.
  • Integrating chemical shift information with predictive algorithms.

Main Results:

  • Accurate determination of conformational changes in protein complexes.
  • Successful application of the method despite small chemical shift perturbations.
  • Improved reliability in predicting structural alterations upon binding.

Conclusions:

  • Chemical shift data can be effectively used to determine protein complex structures.
  • The presented procedure enhances the accuracy of analyzing conformational dynamics.
  • This approach offers a robust solution for structural studies of protein interactions.